IUBMB Enzyme Nomenclature

EC 5.1.3.3

Accepted name: aldose 1-epimerase

Reaction: α-D-glucose = β-D-glucose

Other name(s): mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase

Systematic name: aldose 1-epimerase

Comments: Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose. This enzyme catalyses the first step in galactose metabolism by converting β-D-galactose into α-D-galactose, which is the substrate for EC 2.7.1.6, galactokinase [5,6].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-76-9

References:

1. Bentley, R. and Bhate, D.S. Mutarotase from Penicillium notatum. I. Purification, assay, and general properties of the enzyme. J. Biol. Chem. 235 (1960) 1219-1224. [PMID: 13799037]

2. Bentley, R. and Bhate, D.S. Mutarotase from Penicillium notatum. II. The mechanism of the mutarotation reaction. J. Biol. Chem. 235 (1960) 1225-1233. [PMID: 13799038]

3. Keilin, D. and Hartree, E.F. Biological catalysis of mutarotation of glucose. Biochem. J. 50 (1952) 341-348. [PMID: 14915955]

4. Levy, G.B. and Cook, E.S. A rotographic study of mutarotase. Biochem. J. 57 (1954) 50-55. [PMID: 13159947]

5. Beebe, J.A. and Frey, P.A. Galactose mutarotase: purification, characterization, and investigations of two important histidine residues. Biochemistry 37 (1998) 14989-14997. [PMID: 9778377]

6. Thoden, J.B., Timson, D.J., Reece, R.J. and Holden, H.M. Molecular structure of human galactose mutarotase. J. Biol. Chem. 279 (2004) 23431-23437. [PMID: 15026423]

7. Thoden, J.B., Kim, J., Raushel, F.M. and Holden, H.M. The catalytic mechanism of galactose mutarotase. Protein Sci. 12 (2003) 1051-1059. [PMID: 12717027]

[EC 5.1.3.3 created 1961]


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